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Showing 1–22 of 22 results
Advanced filters: Author: Ernst Bamberg Clear advanced filters
  • Fusing light-activated proteins for precise optogenetic control

    • Monya Baker
    • Ernst Bamberg
    News
    Nature Methods
    Volume: 8, P: 985
  • On the anniversary of the Boyden et al. (2005) paper that introduced the use of channelrhodopsin in neurons, Nature Neuroscience asks selected members of the community to comment on the utility, impact and future of this important technique.

    • Antoine Adamantidis
    • Silvia Arber
    • Rachel I Wilson
    Comments & Opinion
    Nature Neuroscience
    Volume: 18, P: 1202-1212
  • Rhodopsin genes have been identified in some large double-stranded DNA viruses, but the structure and functions of viral rhodopsins remain unknown. Here authors present crystal structure and characterization of an Organic Lake Phycodnavirus rhodopsin II (OLPVRII) which forms a pentamer and is a weak proton pump.

    • Dmitry Bratanov
    • Kirill Kovalev
    • Valentin Gordeliy
    ResearchOpen Access
    Nature Communications
    Volume: 10, P: 1-13
  • Optogenetic applications would benefit from channelrhodopsins (ChRs) with faster photostimulation, increased tissue transparency and lower phototoxicity. Here, the authors develop fast red-shifted ChR variants and show the abilities for temporal precise spiking of cerebral interneurons and restoring auditory activity in deaf mice.

    • Thomas Mager
    • David Lopez de la Morena
    • Ernst Bamberg
    ResearchOpen Access
    Nature Communications
    Volume: 9, P: 1-14
  • Molecular engineering allows stoichiometric and co-localized expression of two optogenetic actuators, spaced by a fluorescent protein and an additional transmembrane helix in a single protein fusion. The method provides modular optogenetic tools for bidirectional membrane potential control or synergistic effects on neuronal activity.

    • Sonja Kleinlogel
    • Ulrich Terpitz
    • Ernst Bamberg
    Research
    Nature Methods
    Volume: 8, P: 1083-1088
  • Rhodopsins are ubiquitous light-driven membrane proteins that have diverse functions in nature, and value as optogenetics tools. Here the authors characterise type 1 viral channelrhodopsins, showing that they regulate intracellular calcium and can be used for the photocontrol of muscle contraction in vivo.

    • Ana-Sofia Eria-Oliveira
    • Mathilde Folacci
    • Michel Vivaudou
    ResearchOpen Access
    Nature Communications
    Volume: 15, P: 1-11
  • A light-activated chloride pump that occurs naturally in bacteria can be transfected into neurons, thereby permitting inhibition of neural activity on a millisecond timescale. This complements an existing tool for activating neurons through a photoactivatable algal channel.

    • Feng Zhang
    • Li-Ping Wang
    • Karl Deisseroth
    Research
    Nature
    Volume: 446, P: 633-639
  • Nucleocytoplasmic Large DNA Viruses (NCLDV) that infect algae encode two distinct families of microbial rhodopsins. Here, the authors characterise two proteins form the viral rhodopsin group 1 OLPVR1 and VirChR1, present the 1.4 Å crystal structure of OLPVR1 and show that viral rhodopsins 1 are light-gated cation channels.

    • Dmitrii Zabelskii
    • Alexey Alekseev
    • Valentin Gordeliy
    ResearchOpen Access
    Nature Communications
    Volume: 11, P: 1-16
  • The Na+-pumping KR2 rhodopsin from Krokinobacter eikastus is a light-driven non-proton cation pump whose mechanism of pumping remains to be understood. Here authors solved crystal structures of the O-intermediate state of the pentameric form of KR2 and its D116N and H30A mutants, which sheds light on the mechanism of non-proton cation light-driven pumping.

    • Kirill Kovalev
    • Roman Astashkin
    • Valentin Gordeliy
    ResearchOpen Access
    Nature Communications
    Volume: 11, P: 1-11
  • Using structural, functional and spectroscopic investigations of a bacterial inward proton-pumping rhodopsin, Kovalev et al. reveal its molecular mechanism and show how proton wires mediate ion selectivity and direct proton transport through cell membrane.

    • Kirill Kovalev
    • Fedor Tsybrov
    • Valentin Gordeliy
    Research
    Nature Structural & Molecular Biology
    Volume: 30, P: 970-979
  • Crystal structures of the microbial rhodopsin KR2, a recently discovered light-driven sodium pump, reveal the translocation pathway of sodium ions and shed light on the molecular mechanism of ion pumping.

    • Ivan Gushchin
    • Vitaly Shevchenko
    • Valentin Gordeliy
    Research
    Nature Structural & Molecular Biology
    Volume: 22, P: 390-395
  • In this Technical Report, Kleinlogel and colleagues created and characterized a new channelrhodopsin-2 mutant with an enhanced permeability to calcium. Dubbed CatCh (calcium translocating channelrhodopsin), this new variant's enhanced calcium permeability mediates an accelerated response time and voltage response that is ~70-fold more light sensitive than that of wild-type channelrhodopsin-2.

    • Sonja Kleinlogel
    • Katrin Feldbauer
    • Ernst Bamberg
    Research
    Nature Neuroscience
    Volume: 14, P: 513-518
  • In the retina, highly selective wiring from inhibitory cells contributes to determine the direction-selection characteristics of an individual ganglion cell, yet how the asymmetric wiring inherent to these connections is established was unknown. Here, two independent studies using complementary techniques, including pharmacology, electrophysiology and optogenetics, find that although inhibitory inputs to both sides of the direction-selective cell are uniform early in development, by the second postnatal week, inhibitory synapses on the null side strengthen whereas those on the preferred side remain constant. These plasticity changes occur independent of neural activity, indicating that a specific developmental program is executed to produce the direction-selective circuitry in the retina.

    • Keisuke Yonehara
    • Kamill Balint
    • Botond Roska
    Research
    Nature
    Volume: 469, P: 407-410
  • Proteorhodopsins act as light-driven outward proton pumps mainly at neutral and alkaline pH, however, mirror proteorhodopsins are known to operate only at acidic pH. Here, the authors report the detailed structural and functional characterization of pH mirror proteorhodopsin SpaR as well as its diverse biological roles.

    • Ivan S. Okhrimenko
    • Kirill Kovalev
    • Valentin I. Gordeliy
    ResearchOpen Access
    Communications Chemistry
    Volume: 6, P: 1-16
  • Zabelskii et al. present a structural and functional analysis of the lightdriven proton pump LR (Mac) from the fungus Leptosphaeria maculans. Their findings indicate that the archaeal ancestry of eukaryotic type 1 rhodopsins, and that the archaeal host of the proto-mitochondrial endosymbiont was capable of light-driven proton pumping.

    • Dmitrii Zabelskii
    • Natalia Dmitrieva
    • Valentin Gordeliy
    ResearchOpen Access
    Communications Biology
    Volume: 4, P: 1-12